Structure of PDB 6hwf Chain N

Receptor sequence
>6hwfN (length=196) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAA
DTQAIADIVQYHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVA
GYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEE
TVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL
3D structure
PDB6hwf Structure-Based Design of Inhibitors Selective for Human Proteasome beta 2c or beta 2i Subunits.
ChainN
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T1 D17 R19 K33 G47 S129 D166 S169
Catalytic site (residue number reindexed from 1) T1 D17 R19 K33 G47 S129 D166 S169
Enzyme Commision number 3.4.25.1: proteasome endopeptidase complex.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GQK N T1 T20 T21 T31 R45 S46 G47 S48 A49 T94 S168 T1 T20 T21 T31 R45 S46 G47 S48 A49 T94 S168
BS02 MG N I163 D166 S169 I163 D166 S169
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004298 threonine-type endopeptidase activity
GO:0005515 protein binding
Biological Process
GO:0006508 proteolysis
GO:0010499 proteasomal ubiquitin-independent protein catabolic process
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0000502 proteasome complex
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005839 proteasome core complex
GO:0019774 proteasome core complex, beta-subunit complex
GO:0034515 proteasome storage granule

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Cellular Component
External links
PDB RCSB:6hwf, PDBe:6hwf, PDBj:6hwf
PDBsum6hwf
PubMed30657666
UniProtP38624|PSB1_YEAST Proteasome subunit beta type-1 (Gene Name=PRE3)

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